Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Full-length and truncated Kv1.3 K+ channels are modulated by 5-HT1c receptor activation and independently by PKC

Full-length and truncated Kv1.3 K+ channels are modulated by 5-HT1c receptor activation and... AIYAR, STEPHAN GRISSMER, AND K. GEORGE CHANDY California 92717 of Physiology and Biophysics, University of California, Irvine, JAYASHREE Aiyar, Jayashree, Stephan Grissmer, and K. George Chandy. Full-length and truncated Kvl.3 are modulatedby 5-HT1, receptor activation and independently by PKC. Am. J. Physiol. 265 (Cell Physiol. 34): Cl571-Cl578, 1993.-In T-cells, the Shaker-related gene,Kvl.3 encodes the type n K+ channel, whereasthe type 1channel is a product of the Shaw subfamily gene, Kv3.1. Both these genes are also expressed the brain. We have usedthe Xenopus oocyte hetin erologous expressionsystemto study the modulatory effects of serotonin (5-hydroxytryptamine, 5-HT) on both these cloned channels.In oocytes coexpressingthe mouse5-HT1, receptor and mouseKvl.3 channel, addition of 100 nM 5-HT causes a complete and sustainedsuppression Kvl.3 currents in -20 of min. In contrast, 5-HT has no effect on mouseKv3.1 currents when coexpressed with 5-HT1, receptor. The 5-HT-mediated suppression Kvl.3 currents proceedsvia activation of a perof tussistoxin-sensitive G protein and a subsequent rise in intracellular Ca2+, but Ca2+ does not directly block the channel. Protein kinase (PK) C activation is not part of the pathway linking 5-HT1, receptor to Kvl.3 channels. However, phorbol estersindependently suppress Kvl.3 currents. Deletion of the first 146 amino acidsfrom the NH,-terminal, containing putative http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

Full-length and truncated Kv1.3 K+ channels are modulated by 5-HT1c receptor activation and independently by PKC

Loading next page...
 
/lp/the-american-physiological-society/full-length-and-truncated-kv1-3-k-channels-are-modulated-by-5-ht1c-yOAIoSzvYi

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
The American Physiological Society
Copyright
Copyright © 1993 the American Physiological Society
ISSN
0363-6143
eISSN
1522-1563
Publisher site
See Article on Publisher Site

Abstract

AIYAR, STEPHAN GRISSMER, AND K. GEORGE CHANDY California 92717 of Physiology and Biophysics, University of California, Irvine, JAYASHREE Aiyar, Jayashree, Stephan Grissmer, and K. George Chandy. Full-length and truncated Kvl.3 are modulatedby 5-HT1, receptor activation and independently by PKC. Am. J. Physiol. 265 (Cell Physiol. 34): Cl571-Cl578, 1993.-In T-cells, the Shaker-related gene,Kvl.3 encodes the type n K+ channel, whereasthe type 1channel is a product of the Shaw subfamily gene, Kv3.1. Both these genes are also expressed the brain. We have usedthe Xenopus oocyte hetin erologous expressionsystemto study the modulatory effects of serotonin (5-hydroxytryptamine, 5-HT) on both these cloned channels.In oocytes coexpressingthe mouse5-HT1, receptor and mouseKvl.3 channel, addition of 100 nM 5-HT causes a complete and sustainedsuppression Kvl.3 currents in -20 of min. In contrast, 5-HT has no effect on mouseKv3.1 currents when coexpressed with 5-HT1, receptor. The 5-HT-mediated suppression Kvl.3 currents proceedsvia activation of a perof tussistoxin-sensitive G protein and a subsequent rise in intracellular Ca2+, but Ca2+ does not directly block the channel. Protein kinase (PK) C activation is not part of the pathway linking 5-HT1, receptor to Kvl.3 channels. However, phorbol estersindependently suppress Kvl.3 currents. Deletion of the first 146 amino acidsfrom the NH,-terminal, containing putative

Journal

AJP - Cell PhysiologyThe American Physiological Society

Published: Dec 1, 1993

There are no references for this article.